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  1. Article: Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes.

    Nikonorova, Inna A / desRanleau, Elizabeth / Jacobs, Katherine C / Saul, Joshua / Walsh, Jonathon D / Wang, Juan / Barr, Maureen M

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Therapeutic use of tiny extracellular vesicles (EVs) requires understanding cargo loading mechanisms. Here, we used a modular proximity label approach to identify EV cargo associated with the transient potential channel (TRP) polycystin PKD-2 ... ...

    Abstract Therapeutic use of tiny extracellular vesicles (EVs) requires understanding cargo loading mechanisms. Here, we used a modular proximity label approach to identify EV cargo associated with the transient potential channel (TRP) polycystin PKD-2 of
    Language English
    Publishing date 2024-04-18
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.04.17.588758
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: What about the males? the

    Walsh, Jonathon D / Boivin, Olivier / Barr, Maureen M

    Journal of neurogenetics

    2020  Volume 34, Issue 3-4, Page(s) 323–334

    Abstract: Sexual dimorphism is a device that supports genetic diversity while providing selective pressure against speciation. This phenomenon is at the core of sexually reproducing organisms. ...

    Abstract Sexual dimorphism is a device that supports genetic diversity while providing selective pressure against speciation. This phenomenon is at the core of sexually reproducing organisms.
    MeSH term(s) Animal Structures/growth & development ; Animal Structures/innervation ; Animal Structures/ultrastructure ; Animals ; CRISPR-Cas Systems ; Caenorhabditis elegans/anatomy & histology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/physiology ; Cell Cycle Proteins/genetics ; Cilia/chemistry ; DNA-Binding Proteins/physiology ; Disease Models, Animal ; Extracellular Vesicles/physiology ; Hermaphroditic Organisms/physiology ; Hermaphroditic Organisms/ultrastructure ; Humans ; Interneurons/physiology ; Male ; Nervous System/anatomy & histology ; Nervous System/growth & development ; Neuronal Plasticity ; Neurons/classification ; Neurons/physiology ; Neurons/ultrastructure ; Neurotransmitter Agents/physiology ; Nondisjunction, Genetic ; Polycystic Kidney, Autosomal Dominant/genetics ; Sex Characteristics ; Sexual Behavior, Animal/physiology ; TRPP Cation Channels/genetics ; Transcription Factors/physiology
    Chemical Substances Caenorhabditis elegans Proteins ; Cell Cycle Proteins ; DNA-Binding Proteins ; HIM-5 protein, C elegans ; Neurotransmitter Agents ; TRPP Cation Channels ; Transcription Factors ; polycystic kidney disease 1 protein ; polycystic kidney disease 2 protein ; tra-1 protein, C elegans
    Language English
    Publishing date 2020-07-10
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 605543-6
    ISSN 1563-5260 ; 0167-7063
    ISSN (online) 1563-5260
    ISSN 0167-7063
    DOI 10.1080/01677063.2020.1789978
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1878: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Tracking N- and C-termini of C. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles.

    Walsh, Jonathon D / Wang, Juan / DeHart, Molly / Nikonorova, Inna A / Srinivasan, Jagan / Barr, Maureen M

    PLoS genetics

    2022  Volume 18, Issue 12, Page(s) e1010560

    Abstract: The cilium acts as an antenna receiving and sending signals, the latter via extracellular vesicles (EVs). In C. elegans and mammals, the Autosomal Dominant Polycystic Kidney Disease (ADPKD) gene products polycystin-1 (PC1) and polycystin-2 (PC2) localize ...

    Abstract The cilium acts as an antenna receiving and sending signals, the latter via extracellular vesicles (EVs). In C. elegans and mammals, the Autosomal Dominant Polycystic Kidney Disease (ADPKD) gene products polycystin-1 (PC1) and polycystin-2 (PC2) localize to both cilia and EVs, act in the same genetic pathway, and function in a sensory capacity, suggesting ancient conservation. However, the functions of the polycystins on cilia and EVs remain enigmatic. We used our C. elegans model and endogenously fluorescent-tagged LOV-1/polycystin-1 to study LOV-1 processing, trafficking, transport, EV biogenesis, and function in living animals. Super resolution, real time imaging reveals that LOV-1 is processed into N-terminal (NTM) and C-terminal (CTM) forms via a conserved GPCR proteolytic site (GPS). The LOV-1 NTM is secreted into the extracellular matrix and not localized to ciliary tip EVs. In contrast, LOV-1 CTM and PKD-2 are co-trafficked, co-transported, and co-localized in cilia and on environmentally released ciliary EVs. LOV-1 CTM requires PKD-2 for ciliary EV localization, while PKD-2 localizes to ciliary EVs independent of LOV-1. We find that LOV-1 but not PKD-2 is required for chemosensation of an ascaroside mating pheromone. These findings indicate that the polycystins LOV-1 and PKD-2 function together and independently and provide insight to how cargo is selected and packaged in ciliary EVs.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cilia/genetics ; Cilia/metabolism ; Extracellular Vesicles/genetics ; Extracellular Vesicles/metabolism ; TRPP Cation Channels/genetics
    Chemical Substances Caenorhabditis elegans Proteins ; TRPP Cation Channels ; LOV-1 protein, C elegans ; PKD-2 protein, C elegans
    Language English
    Publishing date 2022-12-27
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2186725-2
    ISSN 1553-7404 ; 1553-7390
    ISSN (online) 1553-7404
    ISSN 1553-7390
    DOI 10.1371/journal.pgen.1010560
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Sensory cilia act as a specialized venue for regulated extracellular vesicle biogenesis and signaling.

    Wang, Juan / Nikonorova, Inna A / Silva, Malan / Walsh, Jonathon D / Tilton, Peter E / Gu, Amanda / Akella, Jyothi S / Barr, Maureen M

    Current biology : CB

    2021  Volume 31, Issue 17, Page(s) 3943–3951.e3

    Abstract: Ciliary extracellular vesicle (EV) shedding is evolutionarily conserved. In Chlamydomonas and C. elegans, ciliary EVs act as signaling devices. ...

    Abstract Ciliary extracellular vesicle (EV) shedding is evolutionarily conserved. In Chlamydomonas and C. elegans, ciliary EVs act as signaling devices.
    MeSH term(s) Animals ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cilia/metabolism ; Extracellular Vesicles/metabolism ; Male ; Mammals ; Protein Transport
    Chemical Substances Caenorhabditis elegans Proteins
    Language English
    Publishing date 2021-07-15
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2021.06.040
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3208: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Isolation, profiling, and tracking of extracellular vesicle cargo in Caenorhabditis elegans.

    Nikonorova, Inna A / Wang, Juan / Cope, Alexander L / Tilton, Peter E / Power, Kaiden M / Walsh, Jonathon D / Akella, Jyothi S / Krauchunas, Amber R / Shah, Premal / Barr, Maureen M

    Current biology : CB

    2022  Volume 32, Issue 9, Page(s) 1924–1936.e6

    Abstract: Extracellular vesicles (EVs) may mediate intercellular communication by carrying protein and RNA cargo. The composition, biology, and roles of EVs in physiology and pathology have been primarily studied in the context of biofluids and in cultured ... ...

    Abstract Extracellular vesicles (EVs) may mediate intercellular communication by carrying protein and RNA cargo. The composition, biology, and roles of EVs in physiology and pathology have been primarily studied in the context of biofluids and in cultured mammalian cells. The experimental tractability of C. elegans makes for a powerful in vivo animal system to identify and study EV cargo from its cellular source. We developed an innovative method to label, track, and profile EVs using genetically encoded, fluorescent-tagged EV cargo and conducted a large-scale isolation and proteomic profiling. Nucleic acid binding proteins (∼200) are overrepresented in our dataset. By integrating our EV proteomic dataset with single-cell transcriptomic data, we identified and validated ciliary EV cargo: CD9-like tetraspanin (TSP-6), ectonucleotide pyrophosphatase/phosphodiesterase (ENPP-1), minichromosome maintenance protein (MCM-3), and double-stranded RNA transporter SID-2. C. elegans EVs also harbor RNA, suggesting that EVs may play a role in extracellular RNA-based communication.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Cell Communication ; Extracellular Vesicles/metabolism ; Mammals/genetics ; Proteomics ; RNA
    Chemical Substances RNA (63231-63-0)
    Language English
    Publishing date 2022-03-24
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2022.03.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3208: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: Mutation of NEKL-4/NEK10 and TTLL genes suppress neuronal ciliary degeneration caused by loss of CCPP-1 deglutamylase function.

    Power, Kade M / Akella, Jyothi S / Gu, Amanda / Walsh, Jonathon D / Bellotti, Sebastian / Morash, Margaret / Zhang, Winnie / Ramadan, Yasmin H / Ross, Nicole / Golden, Andy / Smith, Harold E / Barr, Maureen M / O'Hagan, Robert

    PLoS genetics

    2020  Volume 16, Issue 10, Page(s) e1009052

    Abstract: Ciliary microtubules are subject to post-translational modifications that act as a "Tubulin Code" to regulate motor traffic, binding proteins and stability. In humans, loss of CCP1, a cytosolic carboxypeptidase and tubulin deglutamylating enzyme, causes ... ...

    Abstract Ciliary microtubules are subject to post-translational modifications that act as a "Tubulin Code" to regulate motor traffic, binding proteins and stability. In humans, loss of CCP1, a cytosolic carboxypeptidase and tubulin deglutamylating enzyme, causes infantile-onset neurodegeneration. In C. elegans, mutations in ccpp-1, the homolog of CCP1, result in progressive degeneration of neuronal cilia and loss of neuronal function. To identify genes that regulate microtubule glutamylation and ciliary integrity, we performed a forward genetic screen for suppressors of ciliary degeneration in ccpp-1 mutants. We isolated the ttll-5(my38) suppressor, a mutation in a tubulin tyrosine ligase-like glutamylase gene. We show that mutation in the ttll-4, ttll-5, or ttll-11 gene suppressed the hyperglutamylation-induced loss of ciliary dye filling and kinesin-2 mislocalization in ccpp-1 cilia. We also identified the nekl-4(my31) suppressor, an allele affecting the NIMA (Never in Mitosis A)-related kinase NEKL-4/NEK10. In humans, NEK10 mutation causes bronchiectasis, an airway and mucociliary transport disorder caused by defective motile cilia. C. elegans NEKL-4 localizes to the ciliary base but does not localize to cilia, suggesting an indirect role in ciliary processes. This work defines a pathway in which glutamylation, a component of the Tubulin Code, is written by TTLL-4, TTLL-5, and TTLL-11; is erased by CCPP-1; is read by ciliary kinesins; and its downstream effects are modulated by NEKL-4 activity. Identification of regulators of microtubule glutamylation in diverse cellular contexts is important to the development of effective therapies for disorders characterized by changes in microtubule glutamylation. By identifying C. elegans genes important for neuronal and ciliary stability, our work may inform research into the roles of the tubulin code in human ciliopathies and neurodegenerative diseases.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/growth & development ; Caenorhabditis elegans Proteins/genetics ; Carboxypeptidases/genetics ; Carrier Proteins/genetics ; Cilia/genetics ; Cilia/metabolism ; Glutamic Acid/metabolism ; Humans ; Kinesins/genetics ; Microtubules/genetics ; Mutation/genetics ; NIMA-Related Kinases/genetics ; Nerve Degeneration/genetics ; Nerve Degeneration/pathology ; Neurons/metabolism ; Neurons/pathology ; Peptide Synthases/genetics ; Protein Processing, Post-Translational/genetics ; Tubulin/genetics
    Chemical Substances Caenorhabditis elegans Proteins ; Carrier Proteins ; Tubulin ; Glutamic Acid (3KX376GY7L) ; NIMA-Related Kinases (EC 2.7.11.1) ; Nek10 protein, human (EC 2.7.11.1) ; Carboxypeptidases (EC 3.4.-) ; tubulin deglutamylase, C elegans (EC 3.4.-) ; Kinesins (EC 3.6.4.4) ; Peptide Synthases (EC 6.3.2.-) ; TTLL-4 protein, C elegans (EC 6.3.2.-) ; tyrosyltubulin ligase (EC 6.3.2.-)
    Language English
    Publishing date 2020-10-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2186725-2
    ISSN 1553-7404 ; 1553-7390
    ISSN (online) 1553-7404
    ISSN 1553-7390
    DOI 10.1371/journal.pgen.1009052
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: IFT trains in different stages of assembly queue at the ciliary base for consecutive release into the cilium.

    Wingfield, Jenna L / Mengoni, Ilaria / Bomberger, Heather / Jiang, Yu-Yang / Walsh, Jonathon D / Brown, Jason M / Picariello, Tyler / Cochran, Deborah A / Zhu, Bing / Pan, Junmin / Eggenschwiler, Jonathan / Gaertig, Jacek / Witman, George B / Kner, Peter / Lechtreck, Karl

    eLife

    2017  Volume 6

    Abstract: Intraflagellar transport (IFT) trains, multimegadalton assemblies of IFT proteins and motors, traffic proteins in cilia. To study how trains assemble, we employed fluorescence protein-tagged IFT proteins ... ...

    Abstract Intraflagellar transport (IFT) trains, multimegadalton assemblies of IFT proteins and motors, traffic proteins in cilia. To study how trains assemble, we employed fluorescence protein-tagged IFT proteins in
    Language English
    Publishing date 2017-05-31
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.26609
    Database MEDical Literature Analysis and Retrieval System OnLINE

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